Reviewed, UniProtKB/Swiss-Prot B5YW75 (CDD_ECO5E)

Names and origin

Protein names

Recommended name:
    Cytidine deaminase
    EC=3.5.4.5
Alternative name(s):
    Cytidine aminohydrolase
      Short name=CDA

Gene names

Name:	cdd
Ordered Locus Names:	ECH74115_3275

Organism

Escherichia coli O157:H7 (strain EC4115 / EHEC) [Complete proteome] [HAMAP]

Taxonomic identifier

444450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis By similarity.
Catalytic activity	Cytidine + H2O = uridine + NH3. HAMAP MF_01558
Cofactor	Binds 1 zinc ion By similarity.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cytidine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cytidine deaminase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 294	294	Cytidine deaminase HAMAP MF_01558		PRO_1000147096
Regions
	Region	89 – 91	3	Substrate binding By similarity
Sites
	Active site	104	1	Proton donor By similarity
	Metal binding	102	1	Zinc; catalytic By similarity
	Metal binding	129	1	Zinc; catalytic By similarity
	Metal binding	132	1	Zinc; catalytic By similarity

Sequences

	Sequence		Length	Mass (Da)
	B5YW75-1 [UniParc]. Last modified November 25, 2008. Version 1. Checksum: 69B5D87DA4B147DC	FASTA	294	31,541
	10 20 30 40 50 60 MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED ALAFALLPLA 70 80 90 100 110 120 AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT VHAEQSAISH AWLSGEKALA 130 140 150 160 170 180 AITVNYTPCG HCRQFMNELN SGLDLRIHLP GREAHALRDY LADAFGPKDL EIKTLLMDEQ 190 200 210 220 230 240 DHGYALTGDA LSQAAIAAAN RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL 250 260 270 280 290 QGALILLNLK GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHNIDR VLLA

References

[1]	"Complete genome sequence of Escherichia coli O157:H7 str. EC4115." Eppinger M., Sebastian Y., Ravel J. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP001164 Genomic DNA. Translation: ACI36554.1.
RefSeq	YP_002271552.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6970558.
GenomeReviews	Gene locus ECH74115_3275 in contig CP001164_GR.
KEGG	ecf:ECH74115_3275.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	FSPCGHC.
Family and domain databases
HAMAP	MF_01558. [Tree]
InterPro	IPR016192. APOBEC/CMP_deaminase_Zn-bd. IPR002125. CMP_dCMP_Zn_bd. IPR013171. Cyd/dCyd_deaminase_Zn_bd. IPR006263. Cyt_deam_dimer. [Graphical view]
Pfam	PF00383. dCMP_cyt_deam_1. 1 hit. PF08211. dCMP_cyt_deam_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR01355. cyt_deam_dimer. 1 hit.
PROSITE	PS00903. CYT_DCMP_DEAMINASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CDD_ECO5E

Accession

Primary (citable) accession number: B5YW75

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	November 25, 2008
Last modified:	November 3, 2009
This is version 11 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)